Posted on 04/20/2004 7:57:14 PM PDT by PatrickHenry
Red-blooded genealogists take note: The discovery in microbes of two oxygen-packing proteins, the earliest known ancestors to hemoglobin, brings scientists closer to identifying the earliest life forms to use oxygen.
According to the projects lead investigator, University of Hawaii microbiologist Maqsudul Alam, the research may also aid in the search for blood substitutes as new molecular details shed light on how the structure of such proteins, called protoglobins, evolved to transport and release oxygen.
Scientists from the Maui High Performance Computing Center and the University of Texas Southwestern Medical Center contributed to the research. The findings will appear in the Proceedings of the National Academy of Sciences (PNAS) in an online Early Edition this week (at http://www.pnas.org) and in the April 27 print issue. A four-year, $500,000 grant from the National Science Foundation supported the project.
To life on primordial Earth, oxygen was poison. Within single-celled archaea, special proteins arose that captured and transported molecular oxygen, not to release it for respiration but to isolate and detoxify it to protect the organism. Archaea are a distinct group of microbes. Their lineage diverged long ago from a common ancestor they shared with bacteria and eukaryotes (plants, animals and other life forms that encase their DNA within a nucleus). Many strains of archaea exist, often in the planets harshest, hottest and oxygen-deprived environments. Some, however, adapted to use oxygen.
Alams research group found the two primitive protoglobulins in two different archaea species. One, Aeropyrum pernix, is limited to oxygen-based respiration, survives optimally in near-boiling saltwater, and was first discovered among thermal sea vents off Japan. The other, Methanosarcina acetivorans, uses several anaerobic or oxygen-free metabolic pathways that create methane gas. M. acetivorans is found in a wide range of realms, including lake-bottom muck, composting leaves, cow pies and human intestines. The genomes of both have recently been sequenced.
The ability to use oxygen for respiration allowed the diversity of life to expand vastly, an impact more fundamental, if perhaps not as dramatic, as the evolutionary transitions organisms made adapting from sea to land, from the ground to the air, or from all fours to upright.
Elizabeth Hood, who directs the areas of signal transduction and cellular regulation for NSFs Division of Molecular and Cellular Biosciences, said, As early life forms were established on earth, the atmosphere contained numerous toxic molecules, including nitric oxide and hydrogen sulfide. Early hemoglobins most likely evolved to bind and detoxify these gases. When oxygen became a component of the atmosphere, it was also toxic, and these early organisms used hemoglobin to bind and ultimately detoxify the oxygen.
However, for advanced and larger life forms to exist in an oxygen-rich atmosphere on land, a mechanism was needed to take advantage of oxygens benefits, Hood said, and hemoglobins evolved into oxygen carriers rather than detoxifiers.
Finding early hemoglobins in the most primitive life forms on earth testifies to their crucial role in the development of life as we know it today, she said.
(In humans, with each breath in, hemoglobin binds oxygen in the lungs. Then, carried by blood cells made red by its oxygenated presence, the protein transports oxygen to tissues near and far in the body, where it then releases oxygen, which is essential to cellular respiration.)
To find the two protoglobins, the research team used advanced tools of biotechnology and high-performance computing, cloning genetic sequences from the two microbes and using specialized E. coli bacteria as gene-expression machinery to produce samples of the proteins. To analyze their structures, the team compared alignments with other members of the hemoglobin family of compounds. Computers generated models and created molecular dynamic simulations that illustrate with animations how the proteins bind with carbon monoxide, nitric oxide and oxygen.
Genetic sequences, binding characteristics and molecular structures of protoglobins were compared with those of hemoglobins and other oxygen-transport molecules from a wide range of organisms, including bacteria, tubeworms, roundworms, segmented bloodworms, mice, humans and sperm whales.
According to Alam, the similarities between these molecules and the protoglobins of A. pernix and M. acetivorans suggest intriguing connections between them and the evolution of mechanisms that sense oxygen, carbon monoxide, nitric oxide and hydrogen sulfide. These similarities, he said, also suggest connections to LUCA, short-hand for the Last Universal Common Ancestor.
LUCA is believed to have been a metabolically flexible single-celled organism with the ability to utilize oxygen for energy before free oxygen even existed in the air, said Alam. We think protoglobin helped give life to LUCA. And its descendents hemoglobin, myoglobin, neuroglobin, and cytoglobin allowed higher organisms to evolve by allowing organisms to maintain a metabolic balance in an oxygenated world.
(6) is generally their default setting.
Read a biology book - there is none.
From our rung on the evolutionary ladder we can see the simpler life forms that have come before us, but what about higher forms of life?
Higher? Lower? What does that mean?
The most successful form of life is still bacteria.
... The only feature that is absolutely conserved in this subfamily of proteins is the histidine amino acid that binds to the heme iron.Not specifically, just my memory from my old molbio textbooks. Anyway, ID does not expect that an irreducibly complex element be conserved absolutely, amino acid by amino acid, atom by atom, but that functional forms have a minimal complexity.
A frontal view of one heme group shows how the heme group binds the iron atom. The heme groups consists of carbon atoms (grey), nitrogen atoms (blue), oxygen atoms (red stick ends), the iron atom (red ball in the center), and hydrogen atoms (not shown). Notice the blue nitrogen atoms (shown as sticks) directly contact the iron atom. This is an illustration of the coordination mentioned above.
From this side view, it is evident (if you look closely) that the iron atom is slightly out of the plane formed by the heme group. This occurs in the absence of the sixth legand (for example O2 or CO). The next image illustrates how the heme is attached to the peptide chain.
The amino acid histidine that coordinates to the iron atom is now rendered as a "sticks" model. The arrangement of 5 nitrogen atoms around the central iron atom in the coordination complex is called a tetragonal pyramid.
When heme in hemoglobin binds another ligand (for example O2) a new geometry results. In this example, the oxygen molecule is bound directly opposite the nitrogen atom of the histidine group. In the oxy form of hemoglobin, there are 6 ligands to the iron atom. The result is an octahedral complex, that is the atoms around the central iron atom are arranged to form an octahedron. Notice that the iron is now pulled into the plane of the heme group.
Maybe I should restate the question why not "a "GOD" like entity with "supreme intelligence" ...and "power over the physical environment"
Is there any reason the evolutionary process could/would not eventually produce a "Supreme Being" which could possess the attributes of "GOD"? Especially in light of the possibility that man/machine may be able to direct thier future evolution? Thanks for all the responses.
Non Sequitur
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